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Originally published as MBC in Press, 10.1091/mbc.01-10-0514 on February 28, 2002
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Vol. 13, Issue 5, 1778-1791, May 2002

Targeting of Rough Endoplasmic Reticulum Membrane Proteins and Ribosomes in Invertebrate Neurons

Melissa M. Rolls,* David H. Hall,Dagger Martin Victor,§ Ernst H. K. Stelzer,|| and Tom A. Rapoport*

Departments of  *Cell Biology and  §Pathology, Harvard Medical School, Boston, Massachusetts 02115;  Dagger Center for C. elegans Anatomy, Department of Neuroscience, Albert Einstein College of Medicine, Bronx, New York 10461; and  ||Light Microscopy Group and Cell Biophysics Programme, European Molecular Biology Laboratory, D-69117 Heidelberg, Germany

The endoplasmic reticulum (ER) is divided into rough and smooth domains (RER and SER). The two domains share most proteins, but RER is enriched in some membrane proteins by an unknown mechanism. We studied RER protein targeting by expressing fluorescent protein fusions to ER membrane proteins in Caenorhabditis elegans. In several cell types RER and general ER proteins colocalized, but in neurons RER proteins were concentrated in the cell body, whereas general ER proteins were also found in neurites. Surprisingly RER membrane proteins diffused rapidly within the cell body, indicating they are not localized by immobilization. Ribosomes were also concentrated in the cell body, suggesting they may be in part responsible for targeting RER membrane proteins.


Corresponding author. E-mail address: tom_rapoport{at}hms.harvard.edu.

Dagger Present address: Institute of Neuroscience, University of Oregon 1254, Eugene, OR 97403.


Molecular Biology of the Cell
Vol. 13, 1778-1791, May 2002
Copyright © 2002 by The American Society for Cell Biology



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